Isolation and characterization of a new acidophilic Thiobacillus species (T. albertis)

1983 ◽  
Vol 29 (9) ◽  
pp. 1159-1170 ◽  
Author(s):  
R. D. Bryant ◽  
K. M. McGroarty ◽  
J. W. Costerton ◽  
E. J. Laishley
Keyword(s):  
Inclusion Bodies ◽  
Cell Envelope ◽  
Ultrastructural Studies ◽  
Isolation And Characterization ◽  
Sulfur Granule ◽  
Stabilization Procedure ◽  
Membrane Bound ◽  
Sulfur Oxidizing ◽  
Ph Range

An acidophilic, rod-shaped, sulfur-oxidizing bacterium was isolated from extremely acidic soil adjacent to a sulfur stockpile at Fox Creek, Alta. This isolate was found to grow only autotrophically by oxidizing S° and reduced inorganic sulfur compounds (S2O32− and S4O62−), placing it in the genus Thiobacillus. Aerobic growth was observed over a pH range of 2.0 to 4.5 with optimum growth at 3.5 to 4.0. Analysis of its DNA revealed a mol% G + C content of 61.5. Ultrastructural studies showed that the isolate possessed a tuft of polar flagella. A glycocalyx was observed only after the antiserum stabilization procedure, which showed it extending outwards from the outer membrane of the bacterial cell envelope. Cleavage planes of this cell showed a typical Gram-negative cell wall. The cytoplasm contained two types of inclusion bodies, carboxysomes and a single large membrane-bound sulfur granule. This isolate had morphological and physiological characteristics which were not totally comparable with other known acidiophilic thiobacilli demonstrating this bacterium to be a new Thiobacillus sp. named T.albertis.

Isolation and Characterization of Plasminogen Activator from Pig Leucocytes

1974 ◽  
Vol 31 (01) ◽  
pp. 072-085 ◽  
Author(s):  
M Kopitar ◽  
M Stegnar ◽  
B Accetto ◽  
D Lebez
Keyword(s):  
Molecular Weight ◽  
Plasminogen Activator ◽  
Gel Electrophoresis ◽  
Gel Filtration ◽  
Ph Optimum ◽  
Isolation And Characterization ◽  
Ph Range ◽  
Inhibition Studies ◽  
Final Purification

SummaryPlasminogen activator was isolated from disrupted pig leucocytes by the aid of DEAE chromatography, gel filtration on Sephadex G-100 and final purification on CM cellulose, or by preparative gel electrophoresis.Isolated plasminogen activator corresponds No. 3 band of the starting sample of leucocyte cells (that is composed from 10 gel electrophoretic bands).pH optimum was found to be in pH range 8.0–8.5 and the highest pH stability is between pH range 5.0–8.0.Inhibition studies of isolated plasminogen activator were performed with EACA, AMCHA, PAMBA and Trasylol, using Anson and Astrup method. By Astrup method 100% inhibition was found with EACA and Trasylol and 30% with AMCHA. PAMBA gave 60% inhibition already at concentration 10–3 M/ml. Molecular weight of plasminogen activator was determined by gel filtration on Sephadex G-100. The value obtained from 4 different samples was found to be 28000–30500.

scholarly journals Isolation and characterization of a membrane protein from rat erythrocytes which inhibits lysis by the membrane attack complex of rat complement

1992 ◽  
Vol 284 (1) ◽  
pp. 169-176 ◽  
Author(s):  
T R Hughes ◽  
S J Piddlesden ◽  
J D Williams ◽  
R A Harrison ◽  
B P Morgan
Keyword(s):  
Affinity Purification ◽  
Membrane Attack Complex ◽  
Erythrocyte Membranes ◽  
Dependent Manner ◽  
Inhibitory Protein ◽  
Rat Erythrocytes ◽  
Butanol Extract ◽  
Isolation And Characterization ◽  
Membrane Bound

The membrane attack complex (MAC) of complement in humans is regulated by several membrane-bound proteins; however, no such proteins have so far been described in other species. Here we report the isolation and characterization of a rat erythrocyte membrane glycoprotein of molecular mass 21 kDa which inserts into cell membranes and is a potent inhibitor of the rat MAC. This protein, here called rat inhibitory protein (RIP), was first partially purified by column chromatography from a butanol extract of rat erythrocyte membranes. Monoclonal antibodies (Mabs) were raised against RIP and used for its affinity purification. Affinity-purified RIP was shown to inhibit in a dose-dependent manner the cobra venom factor (CVF)-mediated ‘reactive’ lysis of guinea pig erythrocytes by rat complement. Conversely, the anti-RIP MAbs 6D1 and TH9 were shown to markedly enhance the CVF-mediated lysis of rat erythrocytes by rat complement. RIP acted late in the assembly of the MAC (at or after the C5b-8 stage) and was releasable from the membranes of rat erythrocytes by phosphatidylinositol-specific phospholipase C. These features, together with its size, deglycosylation pattern and N-terminal amino acid sequence, lead us to conclude that RIP is the rat homologue of the human MAC-inhibitory protein CD59 antigen.

scholarly journals Isolation and Characterization of a Lectin-like Protein (SBLP) from the Dried Roots of Scutellaria baicalensis (Lamiaceae)

2018 ◽  
Vol 13 (12) ◽  
pp. 1934578X1801301
Author(s):  
Huiqin Wang ◽  
Guanzhen Gao ◽  
Lijing Ke ◽  
Jianwu Zhou ◽  
Pingfan Rao
Keyword(s):  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Scutellaria Baicalensis ◽  
Dependent Manner ◽  
Scutellaria Baicalensis Georgi ◽  
Isolation And Characterization ◽  
Pas Staining ◽  
Ph Range ◽  
Dose Dependent

A novel lectin-like protein with MW 63.2 kDa, designated as SBLP, has been isolated and characterized from the dried roots of Scutellaria baicalensis Georgi (Lamiaceae). SBLP was purified by ammonium sulfate precipitation and anion exchange chromatography. It is a glycoprotein according to a PAS staining assay and consisting of protein (86.0%) and sugar (14.0%). Its N-terminal amino acid sequence was determined as GSAVGFLY by Edman degradation. SBLP showed hemagglutinating activity against human and rooster erythrocytes, which were stable below 60°C and in the pH range of 4 −10. Furthermore, SBLP was found to be stimulated by Ca2+, Na+, Ba2+, Zn2+ ions, which suggested it was a metal-dependent lectin. SBLP inhibited the growth of Fusarium oxysporum f.sp. lycopersici and Alternaria eichhorniae in the a dose-dependent manner, and suppressed the proliferation of HepG2 tumor cells with an IC50 of 1.00 μM. This is the first report of a lectin from Radix Scutellariae.

scholarly journals Isolation and Characterization of Membrane-Bound Arylamidases from Human Placenta and Kidney

1980 ◽  
Vol 104 (1) ◽  
pp. 155-165 ◽  
Author(s):  
Kunio HIWADA ◽  
Taketoshi ITO ◽  
Masako YOKOYAMA ◽  
Tatsuo KOKUBU
Keyword(s):  
Human Placenta ◽  
Isolation And Characterization ◽  
Membrane Bound

Isolation and characterization of a mixotrophic sulfur-oxidizing Thermus scotoductus

Extremophiles ◽  
2001 ◽  
Vol 5 (1) ◽  
pp. 45-51 ◽  
Author(s):  
Sigurlaug Skirnisdottir ◽  
Gudmundur O. Hreggvidsson ◽  
Olle Holst ◽  
Jakob K. Kristjansson
Keyword(s):  
Isolation And Characterization ◽  
Sulfur Oxidizing

Isolation and characterization of a Clostridium sp. with cinnamoyl esterase activity and unusual cell envelope ultrastructure

1999 ◽  
Vol 172 (3) ◽  
pp. 139-149 ◽  
Author(s):  
C. S. McSweeney ◽  
Amanda Dulieu ◽  
Richard I. Webb ◽  
Therese Del Dot ◽  
Linda L. Blackall
Keyword(s):  
Esterase Activity ◽  
Cell Envelope ◽  
Isolation And Characterization ◽  
Cinnamoyl Esterase

Biosynthesis of Spin-Labelled Lipids and Their Use in the Study of Biological Membranes: Isolation and Characterization of Membrane-Bound Spin-Labelled sn-3-Phosphatidic Acid-2-3H Prepared by Enzymatic Incorporation of Spin-Labelled Stearic Acid into sn-Glycero-3-phosphate-2-3H

1974 ◽  
Vol 52 (10) ◽  
pp. 884-893 ◽  
Author(s):  
N. Z. Stanacev ◽  
L. Stuhne-Sekalec ◽  
S. Schreier-Muccillo ◽  
I. C. P. Smith
Keyword(s):  
Phosphatidic Acid ◽  
Spin Label ◽  
Liver Microsomes ◽  
Biological Membranes ◽  
General Application ◽  
Isolation And Characterization ◽  
Spin Resonance ◽  
Membrane Bound ◽  
Guinea Pig Liver Microsomes

Spin-labelled 12-doxylstearic acid was covalently incorporated into sn-glycero-3-phosphate-2-3H yielding sn-3-phosphatidic acid-2-3H, a key intermediate in phospholipid biosynthesis, in a reaction catalyzed by isolated guinea-pig liver microsomes. It was found that at least 17.1% of the obtained sn-3-phosphatidic acid-2-3H contained spin label. Degradation of spin-labelled sn-3-phosphatidic acid-2-3H with the phospholipase A from Crotalus adamanteus yielded both lyso-sn-3-phosphatidic acid-2-3H and free fatty acids which were paramagnetic, establishing that the incorporated 12-doxylstearic acid occupies both sn-1- and sn-2-positions of the biosynthesized sn-3-phosphatidic acid-2-3H.A procedure for the preparation and isolation of biosynthetically spin-labelled radioactive sn-3-phosphatidic acid bound to the microsomal membrane was developed and the concentrations of spin-label and tritium were quantitatively determined. This procedure is believed to have a general application in the study of biological membranes. The electron spin resonance spectra and their quantitation are given and discussed for the spin-labelled sn-3-phosphatidic acid-2-3H in solution and in the membrane-bound form. Some general requirements for covalent spin labelling of biological membranes are discussed.

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